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- W1787847872 abstract "Kinetic hydrate inhibitors (KHIs) are used commercially to inhibit gas hydrate formation and growth in pipelines. However, improvement of these polymers has been constrained by the lack of verified molecular models. Since antifreeze proteins (AFPs) act as KHIs, we have used their solved x-ray crystallographic structures in molecular modeling to explore gas hydrate inhibition. The internal clathrate water network of the fish AFP Maxi, which extends to the protein’s outer surface, is remarkably similar to the {100} planes of structure type II (sII) gas hydrate. The crystal structure of this water web has facilitated the construction of in silico models for Maxi and type I AFP binding to sII hydrates. Here, we have substantiated our models with experimental evidence of Maxi binding to the tetrahydrofuran sII model hydrate. Both in silico and experimental evidence support the absorbance-inhibition mechanism proposed for KHI binding to gas hydrates. Based on the Maxi crystal structure we suggest that the inhibitor adsorbs to the gas hydrate lattice through the same anchored clathrate water mechanism used to bind ice. These results will facilitate the rational design of a next generation of effective green KHIs for the petroleum industry to ensure safe and efficient hydrocarbon flow." @default.
- W1787847872 created "2016-06-24" @default.
- W1787847872 creator A5017390574 @default.
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- W1787847872 date "2015-10-01" @default.
- W1787847872 modified "2023-10-12" @default.
- W1787847872 title "Structural Basis for the Inhibition of Gas Hydrates by α -Helical Antifreeze Proteins" @default.
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- W1787847872 doi "https://doi.org/10.1016/j.bpj.2015.08.041" @default.
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